Ruf S.,SanofiDeutschland GmbH |
Buning C.,SanofiDeutschland GmbH |
Schreuder H.,SanofiDeutschland GmbH |
Linz W.,SanofiDeutschland GmbH |
And 5 more authors.
Future Medicinal Chemistry | Year: 2013
The lysosomal serine carboxypeptidase CatA has a very important and well-known structural function as well as a, so far, less explored catalytic function. A complete loss of the CatA protein results in the lysosomal storage disease galactosialidosis caused by intralysosomal degradation of galactosidase and neuraminidase 1. However, mice with a catalytically inactive CatA enzyme show no signs of this disease. This observation establishes a clear distinction between structural and catalytic functions of the CatA enzyme. Recently, several classes of orally bioavailable synthetic inhibitors of CatA have been identified. Pharmacological studies in rodents indicate a remarkable influence of CatA inhibition on cardiovascular disease progression and identify CatA as a promising novel target for the treatment of heart failure. © 2013 Future Science Ltd.